NADH and NADPH are used in distinct metabolic pathways due to specific enzyme binding requirements
the verdict
SUPPORTED
the evidence backs this
confidence 84/100
NADH and NADPH are utilized in largely distinct metabolic pathways because enzymes have evolved specific structural binding requirements and amino acid residues that preferentially recognize one coenzyme over the other.
Evidence for · 2
Structure of <scp>NADP</scp><sup>+</sup>‐dependent glutamate dehydrogenase from <i>Escherichia coli</i> – reflections on the basis of coenzyme specificity in the family of glutamate dehydrogenases
2013 · cited by 24
Demonstrates that specific structural residues and positively charged binding pockets dictate coenzyme preference for either NAD+ or NADP+.
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More for · 1
Amino acid residues that determine functional specificity of NADP‐ and NAD‐dependent isocitrate and isopropylmalate dehydrogenases
2006 · cited by 8
Identifies specific amino acid residues that determine the functional specificity of enzymes toward either NAD or NADP cofactors.